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tyrB tyrosine aminotransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948563, updated on 2-May-2024

Summary

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Gene symbol
tyrB
Gene description
tyrosine aminotransferase
Primary source
ASAP:ABE-0013278
Locus tag
b4054
See related
ECOCYC:EG11040
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK4046
Summary
tyrB is in the TyrR regulon. [More information is available at EcoGene: EG11040]. Tyrosine aminotransferase (TyrB), also known as aromatic-acid aminotransferase, is a broad-specificity enzyme that catalyzes the final step in tyrosine, leucine, and phenylalanine biosynthesis. [More information is available at EcoCyc: EG11040].
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Genomic context

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Sequence:
NC_000913.3 (4267114..4268307)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene replicative DNA helicase Neighboring gene alanine racemase 1 Neighboring gene uncharacterized protein YjbS Neighboring gene acid phosphatase/phosphotransferase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Enzymatic resolution for the preparation of enantiomerically enriched D-beta-heterocyclic alanine derivatives using Escherichia coli aromatic L-amino acid transaminase. Cho BK, et al. Biotechnol Bioeng, 2004 Nov 20. PMID 15459908
  2. The structural interpretations of residue Ser297 in catalytic efficiency of Escherichia coli phenylalanine aminotransferase. Wu SP, et al. Biochim Biophys Acta, 2003 Apr 11. PMID 12686163
  3. The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase. Islam MM, et al. Biochemistry, 2000 Dec 19. PMID 11112527
  4. Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions. Hayashi H, et al. Biochemistry, 1996 May 28. PMID 8639626
  5. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. Onuffer JJ, et al. Protein Sci, 1995 Sep. PMID 8528072, Free PMC Article

See all (40) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. N-terminus verified by Edman degradation on complete protein
    Title: Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables L-leucine:2-oxoglutarate aminotransferase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables L-phenylalanine:2-oxoglutarate aminotransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables L-tyrosine:2-oxoglutarate aminotransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables L-tyrosine:2-oxoglutarate aminotransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables L-tyrosine:2-oxoglutarate aminotransferase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables aromatic-amino-acid:2-oxoglutarate aminotransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aromatic-amino-acid:2-oxoglutarate aminotransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables pyridoxal phosphate binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables pyridoxal phosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables pyridoxal phosphate binding IEA
Inferred from Electronic Annotation
more info
  
enables transaminase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within L-leucine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in L-phenylalanine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in L-phenylalanine biosynthetic process from chorismate via phenylpyruvate IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within L-phenylalanine biosynthetic process from chorismate via phenylpyruvate IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in aromatic amino acid family biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within aspartate biosynthetic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in tyrosine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
tyrosine aminotransferase
NP_418478.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    4267114..4268307
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418478.1 tyrosine aminotransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418478.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2X1J4N6
    Conserved Domains (1) summary
    PRK09257
    Location:1 → 397
    PRK09257; aromatic amino acid transaminase
Nucleotide Protein
Heading Accession and Version

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